ZIG3_CAEEL
ID ZIG3_CAEEL Reviewed; 251 AA.
AC G5EEY6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Zwei Ig domain protein zig-3 {ECO:0000303|PubMed:11809975};
DE AltName: Full=2 Ig domain protein zig-3 {ECO:0000303|PubMed:11809975};
DE Flags: Precursor;
GN Name=zig-3 {ECO:0000312|WormBase:C14F5.2};
GN ORFNames=C14F5.2 {ECO:0000312|WormBase:C14F5.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAL59608.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11809975; DOI=10.1126/science.1066642;
RA Aurelio O., Hall D., Hobert O.;
RT "Immunoglobulin-domain proteins required for maintenance of ventral nerve
RT cord organization.";
RL Science 295:686-690(2002).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19737747; DOI=10.1534/genetics.109.107441;
RA Benard C., Tjoe N., Boulin T., Recio J., Hobert O.;
RT "The small, secreted immunoglobulin protein ZIG-3 maintains axon position
RT in Caenorhabditis elegans.";
RL Genetics 183:917-927(2009).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=22829780; DOI=10.1371/journal.pgen.1002819;
RA Benard C.Y., Blanchette C., Recio J., Hobert O.;
RT "The secreted immunoglobulin domain proteins ZIG-5 and ZIG-8 cooperate with
RT L1CAM/SAX-7 to maintain nervous system integrity.";
RL PLoS Genet. 8:E1002819-E1002819(2012).
CC -!- FUNCTION: Required for maintaining axon position of PVQ and PVP neurons
CC postembryonically in the ventral nerve cord (VNC) by preventing axons
CC drifting into the opposite side of the VNC that could occur during body
CC growth and movement. {ECO:0000269|PubMed:19737747}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in PVT, AIM and ASI neurons, in vulva and
CC weakly in body wall muscles. {ECO:0000269|PubMed:11809975}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at the late L1 larval stage.
CC {ECO:0000269|PubMed:11809975}.
CC -!- DISRUPTION PHENOTYPE: At the L1 larval stage, display defects in the
CC positioning of the ventral nerve cord (VNC) axons characterized by
CC axons of PVQ and PVP neurons, but not of RMEV, HSN and AVK neurons,
CC drifting into the opposite VNC side (axon flip-over) (PubMed:19737747).
CC These defects are not enhanced in a zig-4 (gk34) mutant background or
CC in zig-4 (gk34) dig-1 (ky188), zig-4 (gk34) sax-7 (nj48) or zig-4
CC (gk34) egl-15 (n484) mutant background (PubMed:19737747). In a zig-1,
CC zig-2, zig-4 or zig-5 or zig-8 mutant background, cell body positioning
CC of ASI and ASH head neurons is normal (PubMed:22829780).
CC {ECO:0000269|PubMed:19737747, ECO:0000269|PubMed:22829780}.
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DR EMBL; AF456250; AAL59608.1; -; mRNA.
DR EMBL; BX284606; CCD63845.1; -; Genomic_DNA.
DR PIR; T15495; T15495.
DR RefSeq; NP_509336.1; NM_076935.5.
DR AlphaFoldDB; G5EEY6; -.
DR SMR; G5EEY6; -.
DR STRING; 6239.C14F5.2; -.
DR EPD; G5EEY6; -.
DR PaxDb; G5EEY6; -.
DR PeptideAtlas; G5EEY6; -.
DR EnsemblMetazoa; C14F5.2.1; C14F5.2.1; WBGene00006980.
DR GeneID; 192088; -.
DR KEGG; cel:CELE_C14F5.2; -.
DR CTD; 192088; -.
DR WormBase; C14F5.2; CE01781; WBGene00006980; zig-3.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00970000196086; -.
DR HOGENOM; CLU_072416_1_0_1; -.
DR InParanoid; G5EEY6; -.
DR OMA; PPIHANI; -.
DR OrthoDB; 1482790at2759; -.
DR PhylomeDB; G5EEY6; -.
DR PRO; PR:G5EEY6; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006980; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR10075; PTHR10075; 3.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Immunoglobulin domain; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..251
FT /note="Zwei Ig domain protein zig-3"
FT /id="PRO_5007661504"
FT DOMAIN 42..144
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 160..244
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 65..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 181..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 251 AA; 27837 MW; A609BBD3D394B07E CRC64;
MLLICISVLA AISAHPLSSG EMRAAVSNLV REIDSTHLTT KPSLKIIEGL EDNTVSTGES
VTLRCDVLST PTGVIYWEKD GQRIQGDKEL NVFEKVLNAM GPTVESGIIT SSYQIPCANL
HHIGSYKCVA TNGHDTVESS AKISVEGQTV KCKSTRRSAP VITMSTESRF ELQDNAATLI
CRADRRANWN WMFEDKKIDF DSGRYELLPS GDLLIRKIQW SDMGSYFCIA HNKYGESRGE
TFLYPTKKHI A